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Description
beta-secretase, also called BACE (beta-site of APP cleaving enzyme), is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease and in the formation of myelin sheaths in peripheral nerve cells. BACE1, also known as memapsin-2, is the major beta-secretase for generation of the 40 or 42 amino-acid-long beta-amyloid peptides that aggregate in the brain of Alzheimer's patients. Extracellular cleavage of APP by BACE1 releases a soluble extracellular fragment and is followed by APP cleavage within its transmembrane domain by gamma-secretase. The second cleavage releases the intracellular domain of APP and beta-amyloid.The immature form of BACE1 contains an N-terminal signal sequence (residues 1-1) followed by a large catalytic domain, a single transmembrane domain (residues 461-77), and a short cytoplasmic domain (residues 478-01). The signal sequence (1-21) is cleaved from the immature form, yielding the proBACE1 protein, which starts at residue 22. The proBACE1 protein is modified by cleavage of 24 N-terminal residues (aa 22-45), producing the mature BACE1 protein.Rabbit Anti-BACE1 (26-45) Polyclonal Antibody is developed in rabbit using a synthetic peptide, IRLPLRSGLGGAPLGLRLPR, corresponding to amino acids 26-45 at the N-terminal of human BACE1.Rabbit Anti-BACE1 (26-45) pAb is highly purified from rabbit antiserum by immunoaffinity chromatography and is supplied as 40 μg aliquots at concentration of 0.5 mg/ml.
Immunogen
A synthetic peptide (KLH-conjugated), IRLPLRSGLGGAPLGLRLPR, corresponding - AA 26-45 at N-terminal of human BACE1